Difference between revisions of "YDR258C"

From SGD-Wiki
Jump to: navigation, search
(Automated import of articles)
(Automated import of articles)
Line 4: Line 4:
 
{|{{Prettytable}} align = 'right' width = '200px'
 
{|{{Prettytable}} align = 'right' width = '200px'
 
|-
 
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YDR258C YDR258C]  
+
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002666 YDR258C]  
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HSP78 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''HSP78 ''
Line 14: Line 14:
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|nowrap| Chr IV:974239..971804
 
|nowrap| Chr IV:974239..971804
 +
|-
 +
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000002666
 
|}
 
|}
 
<br>
 
<br>
'''Description of {{PAGENAME}}:''' Oligomeric mitochondrial matrix chaperone that cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; prevents the aggregation of misfolded matrix proteins; component of the mitochondrial proteolysis system<ref name='S000072044'>Rottgers K, et al. (2002) The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J Biol Chem 277(48):45829-37 {{SGDpaper|S000072044}} PMID 12237310</ref><ref name='S000070276'>Germaniuk A, et al. (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8 {{SGDpaper|S000070276}} PMID 12023279</ref><ref name='S000050221'>Schmitt M, et al. (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86 {{SGDpaper|S000050221}} PMID 8830768</ref><ref name='S000047871'>Moczko M, et al. (1995) The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J Mol Biol 254(4):538-43 {{SGDpaper|S000047871}} PMID 7500331</ref><ref name='S000040952'>Leonhardt SA, et al. (1993) HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13(10):6304-13 {{SGDpaper|S000040952}} PMID 8413229</ref><ref name='S000039663'>Schmitt M, et al. (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14(14):3434-44
+
'''Description of YDR258C:''' Oligomeric mitochondrial matrix chaperone that cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; prevents the aggregation of misfolded matrix proteins; component of the mitochondrial proteolysis system<ref name='S000072044'>Rottgers K, et al. (2002) The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J Biol Chem 277(48):45829-37 {{SGDpaper|S000072044}} PMID 12237310</ref><ref name='S000070276'>Germaniuk A, et al. (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8 {{SGDpaper|S000070276}} PMID 12023279</ref><ref name='S000050221'>Schmitt M, et al. (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86 {{SGDpaper|S000050221}} PMID 8830768</ref><ref name='S000047871'>Moczko M, et al. (1995) The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J Mol Biol 254(4):538-43 {{SGDpaper|S000047871}} PMID 7500331</ref><ref name='S000040952'>Leonhardt SA, et al. (1993) HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13(10):6304-13 {{SGDpaper|S000040952}} PMID 8413229</ref><ref name='S000039663'>Schmitt M, et al. (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14(14):3434-44
 
  {{SGDpaper|S000039663}} PMID 7628444</ref>
 
  {{SGDpaper|S000039663}} PMID 7628444</ref>
 
<br>
 
<br>
Line 37: Line 39:
 
J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
-->
 
-->
 +
 +
  
 
<protect>
 
<protect>

Revision as of 08:46, 27 February 2007

Share your knowledge...Edit this entry! <protect>

Systematic name YDR258C
Gene name HSP78
Aliases
Feature type ORF, Verified
Coordinates Chr IV:974239..971804
Primary SGDID S000002666


Description of YDR258C: Oligomeric mitochondrial matrix chaperone that cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; prevents the aggregation of misfolded matrix proteins; component of the mitochondrial proteolysis system[1][2][3][4][5][6]




</protect>

Community Commentary

About Community Commentary. Please share your knowledge!




<protect>

References

See Help:References on how to add references

  1. Rottgers K, et al. (2002) The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J Biol Chem 277(48):45829-37 SGD PMID 12237310
  2. Germaniuk A, et al. (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8 SGD PMID 12023279
  3. Schmitt M, et al. (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86 SGD PMID 8830768
  4. Moczko M, et al. (1995) The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J Mol Biol 254(4):538-43 SGD PMID 7500331
  5. Leonhardt SA, et al. (1993) HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13(10):6304-13 SGD PMID 8413229
  6. Schmitt M, et al. (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14(14):3434-44 SGD PMID 7628444

See Help:Categories on how to add the wiki page for this gene to a Category </protect>